Heat-shock proteins of Drosophila are associated with nuclease-resistant, high-salt-resistant nuclear structures.
Proteins produced in cultured Drosophila cells during the heat-shock response (HSPs) were recently shown by autoradiography to be confined in large measure to the cell nucleus. We report here that nuclear HSPs are not associated with nucleosomes solubilizes by treatment with staphylococcal nuclease at low ionic strength nor are HSPs released by extraction with high salt, which solubilized most of the remaining histones and DNA. Possible functions of nuclear HSPs are discussed.
D000818:Animals; D002467:Cell Nucleus / Q000032:analysis*; D002478:Cells, Cultured; D004331:Drosophila melanogaster / Q000032:analysis*; D006360:Heat-Shock Proteins; D008836:Micrococcal Nuclease; D009707:Nucleosomes / Q000032:analysis; D011506:Proteins / Q000032:analysis*; D012965:Sodium Chloride / Q000494:pharmacology
D006360:Heat-Shock Proteins; D009707:Nucleosomes; D011506:Proteins; D012965:Sodium Chloride; D008836:Micrococcal Nuclease